ID A0A3Q0SBB1_AMPCI Unreviewed; 1220 AA.
AC A0A3Q0SBB1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=ATP8B1 {ECO:0000313|Ensembl:ENSACIP00000020391.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000020391.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000020391.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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DR STRING; 61819.ENSACIP00000020391; -.
DR Ensembl; ENSACIT00000020927.1; ENSACIP00000020391.1; ENSACIG00000015800.1.
DR GeneTree; ENSGT00940000158002; -.
DR OMA; GSIRLYC; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF48; PHOSPHOLIPID-TRANSPORTING ATPASE IC; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362033};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 65..143
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 891..1144
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1220 AA; 139496 MW; DA8B1BAA5475D4FA CRC64;
YAKMSRPHAD SQGSLGPNDE VMPYSDDETD DELAEESSEE EEEVQPRPPQ PPEEARPQEV
TWKVKANDRA YHKLPEFKKK VFLCIKKSKY SXNAIKTYKY NALTFLPLNL YEQFKRAANV
YFLGLLILQI IPEISTLPWY TTLIPLVIVL GITAIKDLVD DLARHRMDRE INNRKCDVLL
NGRFQEAKWR EIQVGDVVRI KKNDFIPADI LLLSSSNPNS LCYVETAELD GETNLKFKLG
LRVTDERLQE ERQLAEFNAL IECEEPNNRL DKFTGIMQWD RERYPLELDN MLLRGCKMRN
TDWCHGLVIF AGADTKIMKN GGKTRFKRTK IDELMNYMVY TIFALLILVA AGLAIGHTYW
YQYVGANAWY LNDGKDQTPG YRGFLTFWGY IIVLNTMVPI SLYVSVEVIR LGQSKFINWD
LQMYFPEKDT PAKARTTTLN EQLGQIQYIF SDKTGTLTQN IMQFKKCSIA GRNYGTDDEE
INKFSISCQL VDWGWNRYAD KKFPFMDHSL VSHVRSKKDK DATEFFKLLS LCHTVMAEDK
HGELIYQAAS PDEGALVTAA RNFGYVFLSR TQDTITIWEM DQEATYEMLA LLDFNSDRKR
MSIILKFPDG RIRLYCKGAD TVIYERLAPN SRYKETTQSA LDVFANETLR TLCLCYKDIS
AEEYEAWSRK HKEAQVTLSD RDAALDRVYE QIENNLMLIG ATAIEDKLQD GVPETIAKLA
KADIKIWVLT GDKKETAENI GYSCSLLTDD MDIHYGENLT RRQASRRGDP QAFRQAKKKS
SEPFFTGNNK NALIITGGWL VSFIQQPELF ENDRLIDNTA ANIDFVNMAC ECEAVICCRV
TPKQKANVVS LVKKYKKAVT LSIGDGANDV NMIKTADIGV GISGQEGMQA VMSSDYAFAQ
FRYLQRLLLV HGRWSYIRMC KFLRFFFFKN FAFTLVHFWF SFFNGYSAQT AYEDWFITLY
NLAYSSLPVL LVGLLDQDVN DRLSLKFPRL YLPGQQGTLF NYKNFFISLF HGIFVSLIIF
FIPYGAFLQT MGQDGEAPSB YQSFAVVTAS SLVFIVNLQI SLDTSYWTFV NCFAVLGSIA
IYFGXMFDIH SAGIHVIFTS IFTFTGVAPN ALRQPYLWLT IILTVGISLL PVICIQFLSK
TVSPSVGDKV RPELKEEEAK KKPSPFQRGG RSRRSAYAFS HSQGYADLIA SGRSIRRRPP
GRAGPQESIR EHPRREAENI
//
